ADAM3 explained

A disintegrin and metalloprotease 3, or ADAM3, belongs to a family of peptidase proteins referred to as ADAMs. Many of these are solely found in spermatogenic cells, specifically in the anterior portion of capacitated spermatozoa heads. This membrane protein is critical for crucial steps in fertilization such as migration of sperm through the uterus to the oviduct as well as binding to the zona pellucida. Inactivation of ADAM3 is a cause of male infertility.[1]

Numerous studies have detailed that in ADAM3 null mice, the spermatozoa fail to migrate through the utero-tubal junction. Furthermore, knockout of the closely related ADAM1a gene in mice, an estrogen receptor not found in mature spermatozoa, causes loss of surface ADAM3 and decreased zona pellucida binding. Other studies have shown ADAM3-/- mouse spermatozoa fail to show sperm-sperm aggregation, although the significance of this is still unknown. ADAM3 has not yet been found in humans.

[2] [3] [4] [5] [6] [7] [8] [9] [10] [11]

Notes and References

  1. "Adam3 MGI Mouse Gene Detail - MGI:102518 - a Disintegrin and Metallopeptidase Domain 3 (cyritestin)." Adam3 MGI Mouse Gene Detail - MGI:102518 - a Disintegrin and Metallopeptidase Domain 3 (cyritestin). N.p., n.d. Web. 04 Dec. 2016.
  2. Wolfsberg. TG. ADAM, a widely distributed and developmentally regulated gene family encoding membrane proteins with a disintegrin and metalloprotease domain.. Dev Biol. 1995. 169. 1. 378–383. 10.1006/dbio.1995.1152. 7750654. free.
  3. Cho. C. Fertilization defects in sperm from mice lacking fertilin beta.. Science. 1998. 281. 5384. 1857–1859. 10.1126/science.281.5384.1857. 9743500.
  4. Yamaguchi. R. Disruption of ADAM3 impairs the migration of sperm into oviduct in mouse.. Biol Reprod. 2009. 81. 1. 142–146. 10.1095/biolreprod.108.074021. 19339711. free.
  5. Fujihara. Y. GPI-anchored protein complex, LY6K/TEX101, is required for sperm migration into the oviduct and male fertility in mice.. Biol Reprod. 2014. 90. 3. 10.1095/biolreprod.113.112888. 60. 24501175. free.
  6. Yamaguchi. R. Aberrant distribution of ADAM3 in sperm from both angiotensin-converting enzyme (Ace)- and calmegin (Clgn)-deficient mice.. Biol Reprod. 2006. 75. 5. 760–766. 10.1095/biolreprod.106.052977. 16870943. free.
  7. Nishimura. H. Possible function of the ADAM1a/ADAM2 Fertilin complex in the appearance of ADAM3 on the sperm surface.. J Biol Chem. 2004. 279. 33. 34957–34962. 10.1074/jbc.m314249200. 15194697. free.
  8. Ikawa. M. Calmegin is required for fertilin alpha/beta heterodimerization and sperm fertility.. Dev Biol. 2001. 240. 1. 254–261. 10.1006/dbio.2001.0462. 11784061. free.
  9. Hagaman. JR. Angiotensin-converting enzyme and male fertility.. Proc Natl Acad Sci USA. 1998. 95. 5. 2552–2557. 10.1073/pnas.95.5.2552 . 19410. 9482924. 1998PNAS...95.2552H. free.
  10. Han. C. Impaired sperm aggregation in Adam2 and Adam3 null mice.. Fertil. Steril.. 2010. 93. 8. 2754–6. 10.1016/j.fertnstert.2010.03.013. 20400072. free.
  11. Grzmil. P. Human cyritestin genes (CRYN1 and CRYN2) are non-functional.. Biochem J. 2001. 357. Pt 2. 551–556. 10.1042/0264-6021:3570551. 1221984. 11439107.

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